Showing papers by "Sumio Shinoda published in 1992"
TL;DR: It is concluded that S. cerevisiae cystathionine gamma-lyase and E. coli cystATHionine Gamma-synthase are homologous in both structure and in vitro function and proposed that their different in vivo functions are due to the unavailability of O-succinylhomoserine in S. Cerevisiae.
Abstract: A DNA fragment containing the Saccharomyces cerevisiae CYS3 (CYI1) gene was cloned. The clone had a single open reading frame of 1,182 bp (394 amino acid residues). By comparison of the deduced amino acid sequence with the N-terminal amino acid sequence of cystathionine gamma-lyase, CYS3 (CYI1) was concluded to be the structural gene for this enzyme. In addition, the deduced sequence showed homology with the following enzymes: rat cystathionine gamma-lyase (41%), Escherichia coli cystathionine gamma-synthase (36%), and cystathionine beta-lyase (25%). The N-terminal half of it was homologous (39%) with the N-terminal half of S. cerevisiae O-acetylserine and O-acetylhomoserine sulfhydrylase. The cloned CYS3 (CYI1) gene marginally complemented the E. coli metB mutation (cystathionine gamma-synthase deficiency) and conferred cystathionine gamma-synthase activity as well as cystathionine gamma-lyase activity to E. coli; cystathionine gamma-synthase activity was detected when O-succinylhomoserine but not O-acetylhomoserine was used as substrate. We therefore conclude that S. cerevisiae cystathionine gamma-lyase and E. coli cystathionine gamma-synthase are homologous in both structure and in vitro function and propose that their different in vivo functions are due to the unavailability of O-succinylhomoserine in S. cerevisiae and the scarceness of cystathionine in E. coli.
39 citations
TL;DR: VVP was shown to poisess the ability to activate the human system through the same mechanism as that clarified in the guinea pig system, namely, VVP converted both human zymogens and active enzymes to active enzymes, and the then generated kallikrein liberated bradykinin from high molecular‐weight kininogen.
36 citations
TL;DR: A compound with siderophore activity was purified by successive column and thin layer chromatographic procedures from Dowex 1 x 8 extracts of culture supernatants of Vibrio parahaemolyticus AQ 3354 and indicated a prominent ion at m/z 477, probably corresponding to [M + 1] ion.
Abstract: A compound with siderophore activity was purified by successive column and thin layer chromatographic procedures from Dower 1 × 8 extracts of culture supernatants of Vibrio parahaemolyticus AQ 3354. The strain synthesized the compound in culture media containing less than 2 μM added FeCl3. Hydrolysis of the compound yielded alanine, ethanolamine, citric acid and 2-ketoglutaric acid. The 1H-NMR spectrum exhibited the presence of a residue from each of these components in the intact molecule. The fast-atom bombardment mass spectrum of the methyl ester derivative indicated a prominent ion at m/z 477, probably corresponding to [M + 1] ion. Other strains of V. parahaemolyticus were also found to produce this compound when grown in an iron-limited medium.
15 citations
TL;DR: The DABA decarboxylase of Vibrio alginolyticus was purified to electrophoretic homogeneity from this bacterium and showed hyperbolic kinetics, and Ca2+ gave a much higher enzyme activity than Mg2+ as a cationic cofactor.
Abstract: Acinetobacter calcoaceticus ATCC 23055 produces a large amount of 1,3-diaminopropane under normal growth conditions. The enzyme responsible, L-2,4-diaminobutyrate (DABA) decarboxylase (EC 4.1.1.-), was purified to electrophoretic homogeneity from this bacterium. The native enzyme had an M
r of approximately 108000, with a pl of 5.0, and was a dimer composed of identical or nearly identical subunits with apparent M
r 53000. The enzyme showed hyperbolic kinetics with a K
m of 1.59 mM for DABA and 14.6 μM for pyridoxal 5'-phosphate as a coenzyme. The pH optimum was in the range 8.5–8.75, and Ca2+gave a much higher enzyme activity than Mg2+as a cationic cofactor. N-γ-AcetyIDABA, 2,3-diaminopropionic acid, ornithine and lysine were inert as substrates. The enzyme was different in subunit structure, N-terminal amino acid sequence and immunoreactivity from the DABA decarboxylase of Vibrio alginolyticus previously described.
11 citations
TL;DR: Results suggest conservation of DNA sequence of the L‐flagellar gene of vibrios, which was demonstrated by dot blot hybridization test with a DNA probe of HL2 L‐ FlageLLar gene fragment.
Abstract: Lateral (L-) flagella-having vibrios were classified into 13 H-serogroups (flagellar antigen serogroups) by means of H-agglutination test. Vibrio parahaemolyticus was classified into 3 serogroups, HL1 to 3. V. alginolyticus and V. harveyi were classified into 5 and 3 serogroups, respectively, but 2 of those were serogroups common to the both species. V. fluvialis and V. furnissii constituted a same serogroup, HL8. Cross-reactivity between each serogroup was not observed in H-agglutination test, although some cross-reactivity was observed in gel diffusion test. Furthermore, similarity of DNA sequence of L-flagellar structure gene was demonstrated by dot blot hybridization test with a DNA probe of HL2 L-flagellar gene fragment. These results suggest conservation of DNA sequence of the L-flagellar gene of vibrios.
10 citations
TL;DR: In this paper, a flow method was developed by both miniaturizing the common flow-injection apparatus and using the dye association method, which was used to determine mico amounts of proteins with low molecular diffusivity.
8 citations